Term of Award

Fall 2024

Degree Name

Master of Science, Applied Physical Science

Document Type and Release Option

Thesis (open access)

Copyright Statement / License for Reuse

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.

Department

Department of Chemistry and Biochemistry

Committee Chair

Mitch Weiland

Committee Member 1

Nathaniel Shank

Committee Member 2

Mark Vincent Dela Cerna

Abstract

Poly(aspartic acid) (PAA) has emerged as a biodegradable and environmentally friendly alternative to non- biodegradable polycarboxylates. This thesis aims to further advance the understanding of PAA degradation by exploring multiple facets focusing on PAA-DNA interactions, particularly those involving the enzyme PahZ1 from Pedobacter sp. KP-2, and to investigate their physiological relevance and potential role in the evolution of PAA biodegradation enzymes. Additionally, the research characterizes PahZ1 homologs from various bacterial species, including Brevifollis gellanilyticus, Erythrobacter insulae, Sphingomonadales, and Sphingopyxis sp. Root 1497. These efforts have identified four novel homologs capable of degrading PAA. Synthetic oligopeptides were employed to identify potential PahZ1 cleavage sites, with timepoint assays conducted to assess and compare enzymatic activity across these homologs. A concurrent study also investigated the role of arginine residues in PahZ2 enzymes and subsequently employed bioinformatics and experimental approaches to predict putative PahZ2 homologs, potentially expanding and creating a new enzyme family. This research enhances our understanding of PAA degradation across diverse microbial environments, offering insights into the development of environmentally friendly polymer.

Research Data and Supplementary Material

No

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